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PMID: 21966348 Published · ppublish English Journal Article

Structural Chemistry of Human SET Domain Protein Methyltransferases.

Current chemical genomics ·Vol. 5 ·No. Suppl 1 ·2011-00-00 ·Pages 85-94

Schapira M

Abstract

There are about fifty SET domain protein methyltransferases (PMTs) in the human genome, that transfer a methyl group from S-adenosyl-L-methionine (SAM) to substrate lysines on histone tails or other peptides. A number of structures in complex with cofactor, substrate, or inhibitors revealed the mechanisms of substrate recognition, methylation state specificity, and chemical inhibition. Based on these structures, we review the structural chemistry of SET domain PMTs, and propose general concepts towards the development of selective inhibitors.

Keywords
Methyltransferase PMT SET domain epigenetics. histone structure
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Schapira Matthieu
Structural Genomics Consortium, University of Toronto, MaRS Centre, Toronto, Ontario, M5G 1L7, Canada.
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Article Info
Journal
Current chemical genomics
Abbr.
Curr Chem Genomics
ISSN
1875-3973
DOI
10.2174/1875397301005010085
Published
2011-00-00
Epub
2011-00-22
Pages
85-94
Language
English
Region
United Arab Emirates
NLM ID
101513465
PMCID
PMC3178901
External Links
PubMed source DOI: 10.2174/1875397301005010085 PMC Full Text
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